Investigation of the interaction between thallous ions and gramicidin A in dimyristoylphosphatidylcholine vesicles: a thallium-205 NMR equilibrium study.
Investigation of the interaction between thallous ions and gramicidin A in dimyristoylphosphatidylcholine vesicles: a thallium-205 NMR equilibrium study.
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二肉豆蔻酰磷脂酰胆碱囊泡中亚铊离子和短杆菌肽 A 之间相互作用的研究:铊 205 NMR 平衡研究。
DOI:
10.1021/bi00368a040
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发表时间:
1986
期刊:
影响因子:
2.9
通讯作者:
Millett,FS
中科院分区:
文献类型:
--
作者:
Shungu,DC;Hinton,JF;Koeppe2nd,RE;Millett,FS
Department of Chemistry and Biochemistry, University of Arkansas, Fayetteville, Arkansas 72701 Received March 18, 1986; Revised Manuscript Received June 6, 1986 abstract: This study reports the first direct observation of multiple occupancy of the gramicidin A channel by Tl+ ions. 205T1 NMR has been used tostudy the equilibrium binding of Tl+ by gramicidin A incorporated in sonicated dimyristoylphosphatidylcholine vesicles. It is shown that only multiple-channel occupancy can account for the 205T1 chemical shifts measured. The data are analyzed to yield the equilibrium association constants of 450-600 and 5-20 M" 1 for the bindingof the first and the second ions at 34 C, respectively.(jramicidin A, a linear pentadecapeptide antibiotic isolated from Bacillus brevis, has a well-known amino acidsequence (Sarges & Witkop, 1965). In natural and artificial lipid membranes, it dimerizes to form ion-transporting transmembrane channels (Hladky & Haydon, 1970, 1972; Bamberg & Lauger, 1973; Urry, 1971; Veatch & Stryer, 1977; Krasne et al., 1971). The channels exhibit a number of properties that